Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Abolition of substrate-dependent currents by tyrosine mutation in the transmembrane domain of glutamate transporter.

FEBS letters - 24 Mar 1997

Choi I, Chiu S Y

Abstract excerpt

By site-directed mutagenesis we examined the roles of tyrosine residues (Tyr127) in the putative transmembrane domain of rat glutamate transporter (GLAST). When expressed in Xenopus oocytes, Y127F mutant protein, which was localized in plasma membranes of oocytes, completely abolished glutamate uptake currents but did not affect the intrinsic substrate-independent currents. Coexpression of wild type and mutant...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Biological Transport
Share to Carrier Proteins
Share to Immunohistochemistry

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Membrane Glycoproteins

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Recombinant Proteins

Source

Identifiers

PMID: 9089276
DOI: 10.1016/s0014-5793(97)00155-5

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Abolition of substrate-dependent currents by tyrosine mutation in the transmembrane domain of glutamate transporter.PMID 9089276Read ↗

Sulfhydryl modification of cysteine mutants of a neuronal glutamate transporter reveals an inverse relationship between sodium dependent conformational changes and the glutamate-gated anion conductance.Semantic proximity Read ↗

Mutations in transmembrane domains 5 and 7 of the human excitatory amino acid transporter 1 affect the substrate-activated anion channel.Semantic proximity Read ↗

Non-essential roles of cysteine residues in functional expression and redox regulatory pathways for canine glutamate/aspartate transporter based on mutagenic analysis.Semantic proximity Read ↗

Dynamic equilibrium between coupled and uncoupled modes of a neuronal glutamate transporter.Semantic proximity Read ↗

Mechanism of cation binding to the glutamate transporter EAAC1 probed with mutation of the conserved amino acid residue Thr101.Semantic proximity Read ↗

A plant homolog of animal glutamate receptors is an ion channel gated by multiple hydrophobic amino acids.Semantic proximity Read ↗

Amyotrophic lateral sclerosis-linked glutamate transporter mutant has impaired glutamate clearance capacity.Semantic proximity Read ↗

Glutamate acts as a partial inverse agonist to metabotropic glutamate receptor with a single amino acid mutation in the transmembrane domain.Semantic proximity Read ↗

Localization of N-glycosylation sites and functional role of the carbohydrate units of GLAST-1, a cloned rat brain L-glutamate/L-aspartate transporter.Semantic proximity Read ↗

The uncoupled chloride conductance of a bacterial glutamate transporter homolog.Semantic proximity Read ↗

A conserved methionine residue controls the substrate selectivity of a neuronal glutamate transporter.Semantic proximity Read ↗

Vesicular glutamate transporter contains two independent transport machineries.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.